Research workbench
AlphaFold monomer V2.0 prediction for EEF1A lysine and N-terminal methyltransferase homolog (Q29LW1)
Analyse AlphaFold monomer V2.0 prediction for EEF1A lysine and N-terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q29LW1
- Type
- protein
- Length
- 673 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6201a9e6C7E0a5Be321dF722661A310740CA2b8A
- Molecule
- EEF1A lysine and N-terminal methyltransferase homolog
- UniProt
- Q29LW1
- Pockets
- 3 · best druggability 0.81
Structure
1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | EEF1A lysine and N-terminal methyltransferase homolog | protein | 673 | 37% helix, 25% strand | Q29LW1 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1063 | 0.81 | 0.82 | 110 | empty |
| 2 | 796 | 0.77 | 0.81 | 72 | empty |
| 3 | 87 | 0.43 | 0.79 | 17 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q29LW1
- Elsewhere: UniProt Q29LW1 · AlphaFold DB Q29LW1
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